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Display of Functionally Active PHB Depolymerase on Escherichia Coli Cell Surface

✍ Scribed by Tomohiro Hiraishi; Koichi Yamashita; Masafumi Sakono; Jun Nakanishi; Liu-Tzea Tan; Kumar Sudesh; Hideki Abe; Mizuo Maeda

Publisher
John Wiley and Sons
Year
2011
Tongue
English
Weight
352 KB
Volume
12
Category
Article
ISSN
1616-5187

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✦ Synopsis

Abstract

The display of PHB depolymerase (PhaZ~RpiT1~) from R. pickettii T1 on the surface of E. coli JM109 cells is realized using OprI of P. aeruginosa as the anchoring motif. The fusion protein is stably expressed and its surface localization is verified by immunofluorescence microscopy. The displayed PhaZ~RpiT1~ retains its cleaving ability for soluble substrates as well as its ability to adsorb to the PHB surface, and also remains catalycically active in the degradation of insoluble polyester materials, in spite of the possible suppression of the enzyme movement on the polymer surface. The results demonstrate that PhaZ~RpiT1~‐displaying E. coli shows potential for use as a whole‐cell biocatalyst for the production of (R)‐3‐hydroxybutyrate monomers from insoluble PHB materials.magnified image

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